Structures of fungal and plant acetohydroxyacid synthases

Thierry Lonhienne (), Yu Shang Low, Mario D. Garcia, Tristan Croll, Yan Gao, Quan Wang, Lou Brillault, Craig M. Williams, James A. Fraser, Ross P. McGeary, Nicholas P. West, Michael J. Landsberg, Zihe Rao, Gerhard Schenk and Luke W. Guddat ()
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Thierry Lonhienne: The University of Queensland
Yu Shang Low: The University of Queensland
Mario D. Garcia: The University of Queensland
Tristan Croll: University of Cambridge
Yan Gao: ShanghaiTech University
Quan Wang: ShanghaiTech University
Lou Brillault: The University of Queensland
Craig M. Williams: The University of Queensland
James A. Fraser: The University of Queensland
Ross P. McGeary: The University of Queensland
Nicholas P. West: The University of Queensland
Michael J. Landsberg: The University of Queensland
Zihe Rao: ShanghaiTech University
Gerhard Schenk: The University of Queensland
Luke W. Guddat: The University of Queensland

Nature, 2020, vol. 586, issue 7828, 317-321

Abstract: Abstract Acetohydroxyacid synthase (AHAS), also known as acetolactate synthase, is a flavin adenine dinucleotide-, thiamine diphosphate- and magnesium-dependent enzyme that catalyses the first step in the biosynthesis of branched-chain amino acids1. It is the target for more than 50 commercial herbicides2. AHAS requires both catalytic and regulatory subunits for maximal activity and functionality. Here we describe structures of the hexadecameric AHAS complexes of Saccharomyces cerevisiae and dodecameric AHAS complexes of Arabidopsis thaliana. We found that the regulatory subunits of these AHAS complexes form a core to which the catalytic subunit dimers are attached, adopting the shape of a Maltese cross. The structures show how the catalytic and regulatory subunits communicate with each other to provide a pathway for activation and for feedback inhibition by branched-chain amino acids. We also show that the AHAS complex of Mycobacterium tuberculosis adopts a similar structure, thus demonstrating that the overall AHAS architecture is conserved across kingdoms.

Date: 2020
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DOI: 10.1038/s41586-020-2514-3

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